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Gel- and Solid-State-Structure of Dialanine and Diphenylalanine Amphiphiles - The importance of C∙∙∙H Interactions in Gelation.
To investigate the role of the capping group in the solution and solid-state self-assembly of short peptide amphiphiles, dialanine and diphenylalanine have been linked via the N-terminus to a benzene (phenyl) and 3-naphthyl capping groups using five different methylene linkers; (CH₂)n, n = 0-4 for the benezene and three (0, 1 and 2) for the naphthalene capping group. Atomic force microscopy (AFM), oscillatory rheology, circular dichroism (CD) and IR analysis have been employed to understand the properties of these peptide-based hydrogels. Several X-ray structures of these short peptide gelators give useful conformational information regarding packing. A comparison of these solid state structures with their gel state properties yielded greater insights into the process of self-assembly in short peptide gelators, particularly in terms of the important role of C∙∙∙H interactions appear to play in determining if a short aromatic peptide does form a gel or not.
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